Dr Kate Heesom
I run the University’s Proteomics Facility, which focuses on the identification of proteins in complex samples and the analysis of changes in protein expression and post-translational modification between different conditions.
- Mass Spectrometry
- Protein Identification
- Protein Quantitation
- Protein Phosphorylation
Senior Research Fellow (Proteomics Facility Director)Life Sciences Faculty Office
As Director of the University of Bristol Proteomics Facility, I run a core research facility that provides a full range of bespoke proteomics services allowing the isolation, identification and quantitation of proteins of interest for researchers within the University of Bristol and to external academic and industrial clients.
The key services provided by the Facility are:
- Protein identification: we can identify the proteins present in anything from a single gel band up to a total cell lysate or tissue homogenate.
- Quantitative Proteomics (eg. TMT and SILAC) for the analysis of changes in protein levels between different samples or conditions.
- Phospho-Proteomics for the identification of phosphorylated proteins and the analysis of changes in phosphorylation between different samples or conditions.
- Interactome Analysis (eg. AP-MS) for the analysis of protein binding partners.
- Secretome analysis.
- Serum proteomics.
Managing organisational unitBristol Veterinary School
01/01/2018 to 08/06/2021
Journal of Cell Science
- Accepted/In press
SARS-CoV-2 vaccine ChAdOx1 nCoV-19 infection of human cell lines reveals low levels of viral backbone gene transcription alongside very high levels of SARS-CoV-2 S glycoprotein gene transcription
Trade-offs between antibacterial resistance and fitness cost in the production of metallo-b-lactamases by enteric bacteria manifest as sporadic emergence of carbapenem resistance in a clinical setting
Antimicrobial Agents and Chemotherapy
Human adventitial pericytes secrete bioactive factors exerting distinct biological effects on cardiac cells
- Conference abstract